Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mapping the interaction of DNA with the Escherichia coli DNA polymerase clamp loader complex.

Nature structural & molecular biology - 1 Feb 2005

Goedken Eric R, Kazmirski Steven L, Bowman Gregory D, O'Donnell Mike, Kuriyan John

Abstract excerpt

Sliding clamps are loaded onto DNA by ATP-dependent clamp loader complexes. A recent crystal structure of a clamp loader-clamp complex suggested an unexpected mechanism for DNA recognition, in which the ATPase subunits of the loader spiral around primed DNA. We report the results of fluorescence-based assays that probe the mechanism of the Escherichia coli clamp loader and show that conserved residues clustered...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to DNA-Directed DNA Polymerase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Fluorescence Resonance Energy Transfer

Share to Nucleic Acid Conformation

Share to Protein Conformation

Share to Protein Subunits

Share to Substrate Specificity

Source

Identifiers

PMID: 15665871
DOI: 10.1038/nsmb889

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping the interaction of DNA with the Escherichia coli DNA polymerase clamp loader complex.PMID 15665871Read ↗

The Escherichia coli clamp loader can actively pry open the β-sliding clamp.Semantic proximity Read ↗

Replisomal coupling between the α-pol III core and the τ-subunit of the clamp loader complex (CLC) are essential for genomic integrity in Escherichia coli.Semantic proximity Read ↗

Kinetic analysis of PCNA clamp binding and release in the clamp loading reaction catalyzed by Saccharomyces cerevisiae replication factor C.Semantic proximity Read ↗

Mechanism of polymerase collision release from sliding clamps on the lagging strand.Semantic proximity Read ↗

Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader.Semantic proximity Read ↗

Allosteric communication in DNA polymerase clamp loaders relies on a critical hydrogen-bonded junction.Semantic proximity Read ↗

A central swivel point in the RFC clamp loader controls PCNA opening and loading on DNA.Semantic proximity Read ↗

Phenotypes of dnaXE145A Mutant Cells Indicate that the Escherichia coli Clamp Loader Has a Role in the Restart of Stalled Replication Forks.Semantic proximity Read ↗

Stepwise assembly of the human replicative polymerase holoenzyme.Semantic proximity Read ↗

Structure of the human clamp loader bound to the sliding clamp: a further twist on AAA+ mechanismSemantic proximity Read ↗

Strand separation establishes a sustained lock at the Tus-Ter replication fork barrier.Semantic proximity Read ↗

Electrostatic Interactions at the Dimer Interface Stabilize the E. coli β Sliding Clamp.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.